Glyoxalase 1 [Caenorhabditis elegans]
VOC family protein( domain architecture ID 11675439)
vicinal oxygen chelate (VOC) family protein uses a metal center to coordinate a substrate, intermediate, or transition state through vicinal oxygen atoms; similar to Homo sapiens glyoxalase domain-containing protein 4
List of domain hits
Name | Accession | Description | Interval | E-value | |||
VOC super family | cl14632 | vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ... |
3-127 | 9.80e-80 | |||
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC is found in a variety of structurally related metalloproteins, including the type I extradiol dioxygenases, glyoxalase I and a group of antibiotic resistance proteins. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). Type I extradiol dioxygenases catalyze the incorporation of both atoms of molecular oxygen into aromatic substrates, which results in the cleavage of aromatic rings. They are key enzymes in the degradation of aromatic compounds. Type I extradiol dioxygenases include class I and class II enzymes. Class I and II enzymes show sequence similarity; the two-domain class II enzymes evolved from a class I enzyme through gene duplication. Glyoxylase I catalyzes the glutathione-dependent inactivation of toxic methylglyoxal, requiring zinc or nickel ions for activity. The antibiotic resistance proteins in this family use a variety of mechanisms to block the function of antibiotics. Bleomycin resistance protein (BLMA) sequesters bleomycin's activity by directly binding to it. Whereas, three types of fosfomycin resistance proteins employ different mechanisms to render fosfomycin inactive by modifying the fosfomycin molecule. Although the proteins in this superfamily are functionally distinct, their structures are similar. The difference among the three dimensional structures of the three types of proteins in this superfamily is interesting from an evolutionary perspective. Both glyoxalase I and BLMA show domain swapping between subunits. However, there is no domain swapping for type 1 extradiol dioxygenases. The actual alignment was detected with superfamily member cd08358: Pssm-ID: 472697 Cd Length: 127 Bit Score: 236.88 E-value: 9.80e-80
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GLOD4_C | cd16357 | C-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; ... |
135-248 | 5.07e-61 | |||
C-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; Uncharacterized subfamily of the vicinal oxygen chelate (VOC) superfamily contains human glyoxalase domain-containing protein 4 and similar proteins. VOC is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping. : Pssm-ID: 319964 Cd Length: 114 Bit Score: 188.53 E-value: 5.07e-61
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Name | Accession | Description | Interval | E-value | |||||
GLOD4_N | cd08358 | N-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; ... |
3-127 | 9.80e-80 | |||||
N-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; Uncharacterized subfamily of the vicinal oxygen chelate (VOC) superfamily contains human glyoxalase domain-containing protein 4 and similar proteins. VOC is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping. Pssm-ID: 319946 Cd Length: 127 Bit Score: 236.88 E-value: 9.80e-80
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GLOD4_C | cd16357 | C-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; ... |
135-248 | 5.07e-61 | |||||
C-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; Uncharacterized subfamily of the vicinal oxygen chelate (VOC) superfamily contains human glyoxalase domain-containing protein 4 and similar proteins. VOC is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping. Pssm-ID: 319964 Cd Length: 114 Bit Score: 188.53 E-value: 5.07e-61
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PLN02300 | PLN02300 | lactoylglutathione lyase |
4-254 | 3.41e-27 | |||||
lactoylglutathione lyase Pssm-ID: 215169 [Multi-domain] Cd Length: 286 Bit Score: 106.79 E-value: 3.41e-27
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glyox_I | TIGR00068 | lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and ... |
4-124 | 4.30e-21 | |||||
lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and glyoxalase I. Glyoxylase I is a homodimer in many species. In some eukaryotes, including yeasts and plants, the orthologous protein carries a tandem duplication, is twice as long, and hits this model twice. [Central intermediary metabolism, Amino sugars, Energy metabolism, Other] Pssm-ID: 272886 Cd Length: 150 Bit Score: 86.78 E-value: 4.30e-21
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Glyoxalase | pfam00903 | Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily; |
132-248 | 1.85e-11 | |||||
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily; Pssm-ID: 395724 [Multi-domain] Cd Length: 121 Bit Score: 60.15 E-value: 1.85e-11
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GloA | COG0346 | Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ... |
136-249 | 3.73e-09 | |||||
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary metabolites biosynthesis, transport and catabolism]; Pssm-ID: 440115 [Multi-domain] Cd Length: 125 Bit Score: 53.84 E-value: 3.73e-09
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Glyoxalase | pfam00903 | Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily; |
7-122 | 4.43e-07 | |||||
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily; Pssm-ID: 395724 [Multi-domain] Cd Length: 121 Bit Score: 47.83 E-value: 4.43e-07
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GloA | COG0346 | Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ... |
7-120 | 3.42e-06 | |||||
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary metabolites biosynthesis, transport and catabolism]; Pssm-ID: 440115 [Multi-domain] Cd Length: 125 Bit Score: 45.37 E-value: 3.42e-06
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Name | Accession | Description | Interval | E-value | |||||
GLOD4_N | cd08358 | N-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; ... |
3-127 | 9.80e-80 | |||||
N-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; Uncharacterized subfamily of the vicinal oxygen chelate (VOC) superfamily contains human glyoxalase domain-containing protein 4 and similar proteins. VOC is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping. Pssm-ID: 319946 Cd Length: 127 Bit Score: 236.88 E-value: 9.80e-80
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GLOD4_C | cd16357 | C-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; ... |
135-248 | 5.07e-61 | |||||
C-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; Uncharacterized subfamily of the vicinal oxygen chelate (VOC) superfamily contains human glyoxalase domain-containing protein 4 and similar proteins. VOC is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping. Pssm-ID: 319964 Cd Length: 114 Bit Score: 188.53 E-value: 5.07e-61
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PLN02300 | PLN02300 | lactoylglutathione lyase |
4-254 | 3.41e-27 | |||||
lactoylglutathione lyase Pssm-ID: 215169 [Multi-domain] Cd Length: 286 Bit Score: 106.79 E-value: 3.41e-27
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glyox_I | TIGR00068 | lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and ... |
4-124 | 4.30e-21 | |||||
lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and glyoxalase I. Glyoxylase I is a homodimer in many species. In some eukaryotes, including yeasts and plants, the orthologous protein carries a tandem duplication, is twice as long, and hits this model twice. [Central intermediary metabolism, Amino sugars, Energy metabolism, Other] Pssm-ID: 272886 Cd Length: 150 Bit Score: 86.78 E-value: 4.30e-21
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GlxI_Ni | cd16358 | Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other ... |
6-124 | 1.30e-20 | |||||
Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other prokaryotic glyoxalase I that uses nickel as cofactor. Glyoxalase I (also known as lactoylglutathione lyase; EC 4.4.1.5) is part of the glyoxalase system, a two-step system for detoxifying methylglyoxal, a side product of glycolysis. This system is responsible for the conversion of reactive, acyclic alpha-oxoaldehydes into the corresponding alpha-hydroxyacids and involves 2 enzymes, glyoxalase I and II. Glyoxalase I catalyses an intramolecular redox reaction of the hemithioacetal (formed from methylglyoxal and glutathione) to form the thioester, S-D-lactoylglutathione. This reaction involves the transfer of two hydrogen atoms from C1 to C2 of the methylglyoxal, and proceeds via an ene-diol intermediate. Glyoxalase I has a requirement for bound metal ions for catalysis. Eukaryotic glyoxalase I prefers the divalent cation zinc as cofactor, whereas Escherichia coil and other prokaryotic glyoxalase I uses nickel. However, eukaryotic Trypanosomatid parasites also use nickel as a cofactor, which could possibly be explained by acquiring their GLOI gene by horizontal gene transfer. Human glyoxalase I is a two-domain enzyme and it has the structure of a domain-swapped dimer with two active sites located at the dimer interface. In yeast, in various plants, insects and Plasmodia, glyoxalase I is four-domain, possibly the result of a further gene duplication and an additional gene fusing event. Pssm-ID: 319965 [Multi-domain] Cd Length: 122 Bit Score: 84.76 E-value: 1.30e-20
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PRK10291 | PRK10291 | glyoxalase I; Provisional |
9-134 | 5.33e-15 | |||||
glyoxalase I; Provisional Pssm-ID: 182358 Cd Length: 129 Bit Score: 70.05 E-value: 5.33e-15
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Glyoxalase | pfam00903 | Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily; |
132-248 | 1.85e-11 | |||||
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily; Pssm-ID: 395724 [Multi-domain] Cd Length: 121 Bit Score: 60.15 E-value: 1.85e-11
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GloA | COG0346 | Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ... |
136-249 | 3.73e-09 | |||||
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary metabolites biosynthesis, transport and catabolism]; Pssm-ID: 440115 [Multi-domain] Cd Length: 125 Bit Score: 53.84 E-value: 3.73e-09
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Glyoxalase | pfam00903 | Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily; |
7-122 | 4.43e-07 | |||||
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily; Pssm-ID: 395724 [Multi-domain] Cd Length: 121 Bit Score: 47.83 E-value: 4.43e-07
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CatE | COG2514 | Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism]; |
136-252 | 8.53e-07 | |||||
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism]; Pssm-ID: 442004 [Multi-domain] Cd Length: 141 Bit Score: 47.26 E-value: 8.53e-07
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GloA | COG0346 | Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ... |
7-120 | 3.42e-06 | |||||
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary metabolites biosynthesis, transport and catabolism]; Pssm-ID: 440115 [Multi-domain] Cd Length: 125 Bit Score: 45.37 E-value: 3.42e-06
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VOC | cd06587 | vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ... |
136-248 | 5.06e-06 | |||||
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC is found in a variety of structurally related metalloproteins, including the type I extradiol dioxygenases, glyoxalase I and a group of antibiotic resistance proteins. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). Type I extradiol dioxygenases catalyze the incorporation of both atoms of molecular oxygen into aromatic substrates, which results in the cleavage of aromatic rings. They are key enzymes in the degradation of aromatic compounds. Type I extradiol dioxygenases include class I and class II enzymes. Class I and II enzymes show sequence similarity; the two-domain class II enzymes evolved from a class I enzyme through gene duplication. Glyoxylase I catalyzes the glutathione-dependent inactivation of toxic methylglyoxal, requiring zinc or nickel ions for activity. The antibiotic resistance proteins in this family use a variety of mechanisms to block the function of antibiotics. Bleomycin resistance protein (BLMA) sequesters bleomycin's activity by directly binding to it. Whereas, three types of fosfomycin resistance proteins employ different mechanisms to render fosfomycin inactive by modifying the fosfomycin molecule. Although the proteins in this superfamily are functionally distinct, their structures are similar. The difference among the three dimensional structures of the three types of proteins in this superfamily is interesting from an evolutionary perspective. Both glyoxalase I and BLMA show domain swapping between subunits. However, there is no domain swapping for type 1 extradiol dioxygenases. Pssm-ID: 319898 [Multi-domain] Cd Length: 112 Bit Score: 44.44 E-value: 5.06e-06
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GlxI_Zn | cd07233 | Glyoxalase I that uses Zn(++) as cofactor; This family includes eukaryotic glyoxalase I that ... |
7-119 | 9.66e-05 | |||||
Glyoxalase I that uses Zn(++) as cofactor; This family includes eukaryotic glyoxalase I that prefers the divalent cation zinc as cofactor. Glyoxalase I (also known as lactoylglutathione lyase; EC 4.4.1.5) is part of the glyoxalase system, a two-step system for detoxifying methylglyoxal, a side product of glycolysis. This system is responsible for the conversion of reactive, acyclic alpha-oxoaldehydes into the corresponding alpha-hydroxyacids and involves 2 enzymes, glyoxalase I and II. Glyoxalase I catalyses an intramolecular redox reaction of the hemithioacetal (formed from methylglyoxal and glutathione) to form the thioester, S-D-lactoylglutathione. This reaction involves the transfer of two hydrogen atoms from C1 to C2 of the methylglyoxal, and proceeds via an ene-diol intermediate. Glyoxalase I has a requirement for bound metal ions for catalysis. Eukaryotic glyoxalase I prefers the divalent cation zinc as cofactor, whereas Escherichia coil and other prokaryotic glyoxalase I uses nickel. However, eukaryotic Trypanosomatid parasites also use nickel as a cofactor, which could possibly be explained by acquiring their GLOI gene by horizontal gene transfer. Human glyoxalase I is a two-domain enzyme and it has the structure of a domain-swapped dimer with two active sites located at the dimer interface. In yeast, in various plants, insects and Plasmodia, glyoxalase I is four-domain, possibly the result of a further gene duplication and an additional gene fusing event. Pssm-ID: 319900 [Multi-domain] Cd Length: 142 Bit Score: 41.54 E-value: 9.66e-05
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VOC | COG3324 | Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ... |
132-249 | 1.88e-04 | |||||
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function prediction only]; Pssm-ID: 442553 [Multi-domain] Cd Length: 119 Bit Score: 40.39 E-value: 1.88e-04
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GlxI_Ni | cd16358 | Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other ... |
133-249 | 2.10e-04 | |||||
Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other prokaryotic glyoxalase I that uses nickel as cofactor. Glyoxalase I (also known as lactoylglutathione lyase; EC 4.4.1.5) is part of the glyoxalase system, a two-step system for detoxifying methylglyoxal, a side product of glycolysis. This system is responsible for the conversion of reactive, acyclic alpha-oxoaldehydes into the corresponding alpha-hydroxyacids and involves 2 enzymes, glyoxalase I and II. Glyoxalase I catalyses an intramolecular redox reaction of the hemithioacetal (formed from methylglyoxal and glutathione) to form the thioester, S-D-lactoylglutathione. This reaction involves the transfer of two hydrogen atoms from C1 to C2 of the methylglyoxal, and proceeds via an ene-diol intermediate. Glyoxalase I has a requirement for bound metal ions for catalysis. Eukaryotic glyoxalase I prefers the divalent cation zinc as cofactor, whereas Escherichia coil and other prokaryotic glyoxalase I uses nickel. However, eukaryotic Trypanosomatid parasites also use nickel as a cofactor, which could possibly be explained by acquiring their GLOI gene by horizontal gene transfer. Human glyoxalase I is a two-domain enzyme and it has the structure of a domain-swapped dimer with two active sites located at the dimer interface. In yeast, in various plants, insects and Plasmodia, glyoxalase I is four-domain, possibly the result of a further gene duplication and an additional gene fusing event. Pssm-ID: 319965 [Multi-domain] Cd Length: 122 Bit Score: 40.07 E-value: 2.10e-04
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VOC | cd06587 | vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ... |
7-124 | 3.77e-04 | |||||
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC is found in a variety of structurally related metalloproteins, including the type I extradiol dioxygenases, glyoxalase I and a group of antibiotic resistance proteins. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). Type I extradiol dioxygenases catalyze the incorporation of both atoms of molecular oxygen into aromatic substrates, which results in the cleavage of aromatic rings. They are key enzymes in the degradation of aromatic compounds. Type I extradiol dioxygenases include class I and class II enzymes. Class I and II enzymes show sequence similarity; the two-domain class II enzymes evolved from a class I enzyme through gene duplication. Glyoxylase I catalyzes the glutathione-dependent inactivation of toxic methylglyoxal, requiring zinc or nickel ions for activity. The antibiotic resistance proteins in this family use a variety of mechanisms to block the function of antibiotics. Bleomycin resistance protein (BLMA) sequesters bleomycin's activity by directly binding to it. Whereas, three types of fosfomycin resistance proteins employ different mechanisms to render fosfomycin inactive by modifying the fosfomycin molecule. Although the proteins in this superfamily are functionally distinct, their structures are similar. The difference among the three dimensional structures of the three types of proteins in this superfamily is interesting from an evolutionary perspective. Both glyoxalase I and BLMA show domain swapping between subunits. However, there is no domain swapping for type 1 extradiol dioxygenases. Pssm-ID: 319898 [Multi-domain] Cd Length: 112 Bit Score: 39.43 E-value: 3.77e-04
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Blast search parameters | ||||
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